We present a novel statistical mechanics formalism for the theoreticaldescription of the process of protein folding$\leftrightarrow$unfoldingtransition in water environment. The formalism is based on the construction ofthe partition function of a protein obeying two-stage-like folding kinetics.Using the statistical mechanics model of solvation of hydrophobic hydrocarbonswe obtain the partition function of infinitely diluted solution of proteins inwater environment. The calculated dependencies of the protein heat capacitiesupon temperature are compared with the corresponding results of experimentalmeasurements for staphylococcal nuclease and metmyoglobin.
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